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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P61769: Variant p.Asp96Asn

Beta-2-microglobulin
Gene: B2M
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Variant information Variant position: help 96 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Aspartate (D) to Asparagine (N) at position 96 (D96N, p.Asp96Asn). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from medium size and acidic (D) to medium size and polar (N) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In AMYL8; reduced stability; in contrast to the wild-type, the mutant aggregates into fibrils with classic amyloid-like properties under physiologic solvent conditions. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 96 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 119 The length of the canonical sequence.
Location on the sequence: help FSKDWSFYLLYYTEFTPTEK D EYACRVNHVTLSQPKIVKWD The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         FSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWD

Gorilla                       FSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWD

Rhesus macaque                FSKDWSFYLLYYTEFTPNEKDEYACRVNHVTLSGPRTVKWD

Chimpanzee                    FSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWD

Mouse                         FSKDWSFYILAHTEFTPTETDTYACRVKHASMAEPKTVYWD

Rat                           FSKDWSFYILAHTEFTPTETDVYACRVKHVTLKEPKTVTWD

Pig                           FSKDWSFYLLVHTEFTPNAVDQYSCRVKHVTLDKPKIVKWD

Bovine                        FSKDWSFYLLSHAEFTPNSKDQYSCRVKHVTLEQPRIVKWD

Rabbit                        FNKDWSFYLLVHTEFTPNNKNEYSCRVKHVTLKEPMTVKWD

Sheep                         FSKDWSFYLLSHAEFTPNSKDQYSCRVNHVTLTQPKIVKWD

Cat                           FNRDWTFYLLVHTEFTPTVEDEYSCQVNHTTLSEPKVVKWD

Horse                         FSKDWSFYLLVHTDFTPNGVDEYSCRVQHSTLKDPLIVKWD

Chicken                       FNDDWTFQRLVHADFTPSSGSTYACKVEHETLKEPQVYKWD

Xenopus laevis                FQHNWKYYTTKSTHVHIDKGDKVECVVSH---NGNPSKKYR

Zebrafish                     FEKGWQFHLTKSVAFTPEKGDEYTCSVRH--MKETKKFSWE
Sequence annotation in neighborhood: help The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.
TypePositionsDescription
Chain 21 – 119 Beta-2-microglobulin
Chain 22 – 119 Beta-2-microglobulin form pI 5.3
Domain 25 – 113 Ig-like C1-type
Glycosylation 78 – 78 N-linked (Glc) (glycation) lysine; in vitro
Glycosylation 111 – 111 N-linked (Glc) (glycation) lysine; in vitro
Glycosylation 114 – 114 N-linked (Glc) (glycation) lysine; in vitro
Disulfide bond 45 – 100
Mutagenesis 79 – 79 D -> P. Increases tendency towards amyloid formation.
Mutagenesis 80 – 80 W -> G. Decreases tendency towards amyloid formation.
Mutagenesis 80 – 80 W -> V. Increases tendency towards amyloid formation.



Literature citations
Hereditary systemic amyloidosis due to Asp76Asn variant beta2-microglobulin.
Valleix S.; Gillmore J.D.; Bridoux F.; Mangione P.P.; Dogan A.; Nedelec B.; Boimard M.; Touchard G.; Goujon J.M.; Lacombe C.; Lozeron P.; Adams D.; Lacroix C.; Maisonobe T.; Plante-Bordeneuve V.; Vrana J.A.; Theis J.D.; Giorgetti S.; Porcari R.; Ricagno S.; Bolognesi M.; Stoppini M.; Delpech M.; Pepys M.B.; Hawkins P.N.; Bellotti V.;
N. Engl. J. Med. 366:2276-2283(2012)
Cited for: INVOLVEMENT IN AMYL8; VARIANT AMYL8 ASN-96; CHARACTERIZATION OF VARIANT AMYL8 ASN-96;
Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.